Structural Basis of Transcription Activation: The CAP-αCTD-DNA Complex

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Science  30 Aug 2002:
Vol. 297, Issue 5586, pp. 1562-1566
DOI: 10.1126/science.1076376

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The Escherichia coli catabolite activator protein (CAP) activates transcription at Plac, Pgal, and other promoters through interactions with the RNA polymerase α subunit carboxyl-terminal domain (αCTD). We determined the crystal structure of the CAP-αCTD-DNA complex at a resolution of 3.1 angstroms. CAP makes direct protein-protein interactions with αCTD, and αCTD makes direct protein-DNA interactions with the DNA segment adjacent to the DNA site for CAP. There are no large-scale conformational changes in CAP and αCTD, and the interface between CAP and αCTD is small. These findings are consistent with the proposal that activation involves a simple “recruitment” mechanism.

  • * Present address: CRC Biomolecular Structure Unit, Institute of Cancer Research, London SW3 6JB, UK.

  • Present address: Tularik Inc., South San Francisco, CA 94080, USA.

  • Present address: Human Genome Sciences Inc., Rockville, MD 20874, USA.

  • § To whom correspondence on crystallographic issues should be addressed. E-mail: berman{at}

  • || To whom correspondence on all other issues should be addressed. E-mail: ebright{at}

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